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首页> 外文期刊>Biochemistry >Study of α-Crystallin Structure by Small Angle Neutron Scattering with ContrastVariation
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Study of α-Crystallin Structure by Small Angle Neutron Scattering with ContrastVariation

机译：小角度中子散射对比研究α-晶体结构

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The structure of the oligomeric protein α-crystallin from bovine eye lens was investigated by small-angle neutron scattering (SANS) with contrast variation. Based on the SANS curves, the match point for α-crystallin (43% D2O) and its average scattering length density at this point (2.4·10~(-1) cm~(-2)) were evaluated. The radius of gyration and the distance distribution functions for α-crystallin were calculated. On the basis of these calculations, it was concluded that α-crystallin is characterized by homogeneous distribution of scattering density in the domains inaccessible for water penetration, and all polypeptide subunits in α-crystallin oligomers undergo equal deuteration. The latter indicates that all α-crystallin subunits are equally accessible for water and presumably for some other low molecular weight substances. These conclusions on the α-crystallin structure (homogeneous distribution of scattering density and equal accessibility of all subunits for low molecular weight substances) should be taken into account when elaborating α-crystallin quaternary structure models.
机译：通过具有对比度变化的小角度中子散射（SANS）研究了牛眼晶状体的寡聚蛋白α-晶体蛋白的结构。根据SANS曲线，评估了α-晶状蛋白（43％D2O）的匹配点及其在该点的平均散射长度密度（2.4·10〜（-1）cm〜（-2））。计算了α-晶状体蛋白的回转半径和距离分布函数。基于这些计算，可以得出结论，α-晶状蛋白的特征在于散射密度在水无法渗透的区域中的均匀分布，并且α-晶状蛋白低聚物中的所有多肽亚基都具有相同的氘代。后者表明，所有α-晶状蛋白亚基都可同等地与水接触，大概对某些其他低分子量物质也可接触。在阐述α-晶状蛋白四元结构模型时，应考虑到有关α-晶状蛋白结构的结论（散射密度的均匀分布和所有亚基对于低分子量物质的可及性）。

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